Mutations to the V-ATPase 'a4' or 'B1' isoforms result in distal renal tubular acidosis, a condition that leads to metabolic acidosis, in some cases with sensorineural deafness.
Subunit F is a 16 kDa protein that is required for the assembly and activity of V-ATPase, and has a potential role in the differential targeting and regulation of the enzyme for specific organelles.
ATPase | V-ATPase | P-type ATPase | Na+/K+-ATPase |
#F-ATPase: mitochondrial ATP synthase, chloroplast ATP synthase
The protein encoded by this gene belongs to the family of P-type cation transport ATPases.
The epsilon subunit is located in the stalk region of the F1 complex, and acts as an inhibitor of the ATPase catalytic core.
V-ATPase 116 kDa isoform a2 is a subunit of the vacuolar ATPase (v-ATPase), an heteromultimeric enzyme that is present in intracellular vesicles and in the plasma membrane of specialized cells, and which is essential for the acidification of diverse cellular components.
The genome encodes several subunits of NADH dehydrogenase (complex I) but lacks all trace of genes for cytochrome and ATPase subunits (Complexes III-V).
It has weak ATPase activity, and binding of ATP leads to the formation of tertiary structures on the surface of the molecule.
It is a microtubule-dependent motor ATPase and has been reported to be involved in the movement of respiratory cilia.
Efrapeptins are peptides made by Tolypocladium that have antifungal, insecticidal, and mitochondrial ATPase inhibitory activities.
In this way a great deal has been learned in recent years about the mechanochemical coupling in the enzymes responsible for muscle contraction, transport in the cell, energy generation (F1-ATPase), DNA replication and transcription (polymerases), DNA unknotting and unwinding (topoisomerases and helicases), and so on.
Aldolase has also been implicated in many "moonlighting" or non-catalytic functions, based upon its binding affinity for multiple other proteins including F-actin, α-tubulin, light chain dynein, WASP, Band 3 anion exchanger, phospholipase D (PLD2), glucose transporter GLUT4, inositol trisphosphate, V-ATPase and ARNO (a guanine nucleotide exchange factor of ARF6).
Dissipation of the proton gradient is coupled to the phosphorylation of ADP through membrane-bound ATPases.
MsiK, the protein encoded by msiK genes, is the ATPase subunit within certain ABC-type membrane transporter proteins.
This phosphorylation results in higher ATPase activity and the assembly of myosin II filaments.
The protein encoded by this gene is a myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads.
However experiments with patients where the Na+/K+-ATPase had been blocked in the underarm by infusion of the Na+/K+-ATPase-blocker Ouabain, no effect on warm-up was observed.
The encoded protein contains coiled-coil domains and a conserved AAA domain characteristic for ATPases associated with a variety of cellular activities.
The first scientific papers were devoted to ATPases and the use of radioactive isotopes in experimental and clinical studies.
Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes.
Dr. John Walker won the 1997 Nobel Prize for Chemistry for his work on ATPase, for which he carried out studies on one of the SRS beamlines.